ID   DNAK_MALP2              Reviewed;         621 AA.
AC   Q8EUH7;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=MYPE9490;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(2002).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; BA000026; BAC44736.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8EUH7; -.
DR   SMR; Q8EUH7; -.
DR   STRING; 272633.26454408; -.
DR   EnsemblBacteria; BAC44736; BAC44736; BAC44736.
DR   KEGG; mpe:MYPE9490; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_14; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002522; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 2.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..621
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078495"
FT   REGION          596..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         202
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   621 AA;  68526 MW;  2B9718D6019BE68E CRC64;
     MRVLKYMLLY ILYLKSIVKI LRRLNNMAGS NIIIGIDLGT TNSCVAVMEN GKSKILETPE
     GKRTIPSVVA FKDNEIIVGD VAKRQMVTNK NTISSIKRLM GTDKTVEVNG KKYTPEQISA
     QILSYIKKCA EEKLGQTITK AVITVPAYFN DAERNATKNA GKIAGLEVER IINEPTAAAL
     AYGMDKSKTE HKVLVYDLGG GTFDVSILEI ADGTFEVLST SGDNHLGGDD WDQKIINWIV
     EEVKKNDKVD LSNDKMAMQR LKDAAEKAKI DLSGLKEVEI SLPFIAMTES GPLNVDLKLT
     RAKFEDLTRD LLERTIKPVE DALKEAKLSA SDIHKVLLVG GSTRMPAVEE LVKSKLGKSP
     DKNINPDEVV AAGAAIQGGV LMGDVKDILL LDVTPLTLSI ETMGGVSTPL IKRNSTIPIS
     KSQIFSTAAD NQPAVDVHVL QGERQMAADN KSLGRFILDG IEPAPRGVPQ IEITFNIDAN
     GILNVKAVDK KTNKEATITI KDSSGLSQEE IDKMIKEAEE NKEKDAQLKE QQEIRYKAES
     LINMFKTSLN GEEGKKVDAK QKEEAEKMIN EFETLLKEEK WDELKTKINQ FEAMASQFAQ
     AAKQNEEKKE EDKKDSEESK N